Protein Variants | Comment | Organism |
---|---|---|
Y229F | the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity | Sulfurisphaera tokodaii |
Y348F | the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value | Sulfurisphaera tokodaii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.027 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y229F | Sulfurisphaera tokodaii | |
0.027 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, wild-type enzyme | Sulfurisphaera tokodaii | |
0.036 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y348F | Sulfurisphaera tokodaii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfurisphaera tokodaii | F9VMT6 | - |
- |
Sulfurisphaera tokodaii 7 | F9VMT6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate + H2O | the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions | Sulfurisphaera tokodaii | D-fructose 6-phosphate + phosphate | - |
r | |
D-fructose 1,6-bisphosphate + H2O | the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions | Sulfurisphaera tokodaii 7 | D-fructose 6-phosphate + phosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
FBP aldolase/phosphatase | bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 | Sulfurisphaera tokodaii |
FBPA/P | bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 | Sulfurisphaera tokodaii |
fructose-1,6-bisphosphate aldolase/phosphatase | bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 | Sulfurisphaera tokodaii |
STK_03180 | locus name. The bifunctional enzyme also shows activity of EC 4.1.2.13 | Sulfurisphaera tokodaii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
48 | - |
assay at | Sulfurisphaera tokodaii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.26 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y348F | Sulfurisphaera tokodaii | |
0.62 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, wild-type enzyme | Sulfurisphaera tokodaii | |
0.66 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y229F | Sulfurisphaera tokodaii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Sulfurisphaera tokodaii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
7.2 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y348F | Sulfurisphaera tokodaii | |
23 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, wild-type enzyme | Sulfurisphaera tokodaii | |
25 | - |
D-fructose 1,6-bisphosphate | pH 7.8, 48°C, mutant enzyme Y229F | Sulfurisphaera tokodaii |